Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Anti-tie2 antibody and use thereof

A TIE-2 and antibody technology, applied in the direction of antibodies, antibody medical components, applications, etc., can solve the problems of reduced drug accessibility and reduced therapeutic effect

Pending Publication Date: 2022-01-28
PHARMABCINE
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Thus, even when a therapeutic agent is used to treat a tumor, the therapeutic effect is reduced due to the reduced accessibility of the drug to the interior of the tissue (Gianfranco Baronzio et al., Frontiers in Oncology. 5:165, 2015)

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Anti-tie2 antibody and use thereof
  • Anti-tie2 antibody and use thereof
  • Anti-tie2 antibody and use thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0122] Example 1 Screening of Antibodies Binding to TIE2

[0123] A human primary ScFv (scFv) library disclosed in Korean Patent Laid-Open Publication No. 10-2008-0109417 was used to screen for antibodies binding to TIE2 and to prepare the library. Spread 100 μl of antigen (hTIE2-his: Sino Biological, 10700-H08H) on 96-well Ni at 2 μl / ml + plate and incubate overnight at 4°C. The next day, the antigen-coated plate was washed three times with 0.1% TBST, and then reacted with 200 μl of 2% BSA blocking buffer for 2 hours at room temperature. Add 50 μl of XL1-Blue stock solution to 2 ml of 2xYT-TET (tetracycline 10 μg / ml) growth medium, and incubate at 37°C at 200 rpm for 2 hours, then add 13 ml of 2xYT-TET growth medium, and Incubate until OD 600 reach 0.5. After blocking for 2 hours, the wells were washed 3 times with 1XPBS. The phage library group was combined with each washed well, the phage library was mixed with 4% BSA in equal amounts, and then 200 µl of the mixture wa...

Embodiment 2

[0124] Example 2 Screening of monoclonal ScFv phage that specifically binds to TIE2 and neutralizes the binding to TIE2 (combination ELISA)

[0125] After completing the panning process, the final circular cell stock solution was diluted to form 200 to 500 colonies, plated on CM agar plates, and then incubated overnight at 37 °C. The next day, when the colony grows, add 200 μl of 2xYT medium (CM 34 μg / ml+1% glucose) into a 96-well deep-well plate, insert one colony into each well, and then place the plate at 37°C and 3,000rpm Incubate overnight. The next day, spread 200 μl of 2xYT medium (CM 34 μg / ml+1% glucose) on a fresh 96-well deep-well plate, inject 20 ml of the cells grown the day before into each well, and incubate at 37°C and 3,000 Grow for 1 hour and 10 minutes at rpm. Store the remaining cells in 100 μl of 50% glycerol at -70 °C. While the cells were growing, mix 1 μl of helper phage with 19 μl of 2xYT medium, inject 20 μl of the resulting mixture into each well, ...

Embodiment 3

[0141] Example 3 Selection of antibodies with binding ability to cells expressing TIE2

[0142] To determine binding to TIE2-expressing cells, binding to self-established human / mouse TIE2-overexpressing CHO-K1 cell lines (hTIE2 / CHO-K1, mTIE2 / CHO-K1) was measured using flow cytometry. Each cell line was maintained and cultured, hTIE2 CHO-K1 was washed with PBS, 5 mM EDTA was added thereto to obtain a cell suspension, and each cell was recovered by centrifugation. Prepare 5×10 cells in FACS-specific buffer (PBS containing 2% FBS, 0.05% sodium azide) 6 cells / mL of cell suspension, and dispense 100 μL of cell suspension into each tube. Add 100 µL of 2 µg / mL clones to each tube and let stand at 4 °C for 30 min to induce cell binding. The cells were washed with 2 mL of FACS buffer, 100 μL of secondary antibody dilution (1 / 500, anti-human IgG-Fc polyclonal antibody fragment conjugated with PE, #A80-248PE, BethylLaboratories Inc.US) was added to it, and the resulting The mixture wa...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The present invention relates to an antibody, which specifically binds to tyrosine-protein kinase receptor TIE-2 (TIE2) so as to possess functions of blood vessel normalization and stabilization through receptor phosphorylation, and relates to: an anti-TIE2 antibody; a nucleic acid encoding same; a vector comprising the nucleic acid; a cell transformed with the vector; a method for preparing the antibody; an agent for stabilizing blood vessels and a composition for treating angiogenesis-associated diseases, both of which comprise the antibody; and a composition for co-administration with a pharmaceutical composition for tumor or cancer treatment and with a composition other than an antibody binding to TIE2.

Description

technical field [0001] The present invention relates to an antibody that specifically binds to TIE2 (tyrosine kinase receptor) and has a function of normalizing and stabilizing blood vessels through phosphorylation of the receptor. More specifically, the present invention relates to an anti-TIE2 antibody, a nucleic acid encoding the antibody, a vector comprising the nucleic acid, a cell transformed with the vector, a blood vessel stabilizer and a , a composition of the blood vessel stabilizer for treating an angiogenesis-related disease, a pharmaceutical composition for treating tumor or cancer, and a composition for administration in combination with a drug other than an antibody that binds to TIE2. Background technique [0002] Angiogenesis is the mechanism by which existing blood vessels form new blood vessels through the growth, division, migration, etc. of endothelial cells, and plays a key role in normal growth processes including wound healing and the female menstrual...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): C07K16/28G01N33/574C12N15/13A61K39/395A61P35/00A61P35/04A61P3/10A61P9/10A61P27/02A61P37/06A61P27/06A61P17/00A61P17/06A61P19/02A61P17/02A61P9/14A61P29/00A61P37/02A61P1/00A61P1/16A61P13/12A61P11/00A61P31/04A61P25/00
CPCC07K16/2863G01N33/574A61K39/3955A61P35/00A61P35/04A61P3/10A61P9/10A61P27/02A61P37/06A61P27/06A61P17/00A61P17/06A61P19/02A61P17/02A61P9/14A61P29/00A61P37/02A61P1/00A61P1/16A61P13/12A61P11/00A61P31/04A61P25/00C07K2317/56C07K2317/565C07K2317/92C07K2317/33C07K2317/76G01N2333/71A61K2039/505A61K2300/00A61K45/06G01N2800/7014G01N2333/515G01N33/6872C07K2317/622A61K2039/55C07K16/005
Inventor 李恩雅朴范用姜努日朴千虎李英爱金度玧李元燮柳珍山
Owner PHARMABCINE
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com